Evidence map›Paper›PMID 33993565›Full record

ArticleFASEB journal : official publication of the Federation of American Societies for Experimental Biology2021

Phenylalanine hydroxylase contributes to serotonin synthesis in mice.

Alexander Mordhorst, Priyavathi Dhandapani, Susann Matthes, Valentina Mosienko, Michael Rothe, Mihail Todiras, Julie Self, Wolf-Hagen Schunck, Anja Schütz, Michael Bader and 1 more

Open access · hybridAbstract read
In one paragraph

Article in FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.5field-weighted citation impact, top 19% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

14 citing papers in PubMed, 18 citations in OpenAlex.

  1. Efavirenz-Altered Gut-Microbiota,International journal of molecular sciences · 2026
    Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Phenylalanine hydroxylase contributes to serotonin synthesis in mice.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2021
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

11 authors at 3 institutions in 3 countries.

Alexander MordhorstMax-Delbrück-Center for Molecular Medicine in the Helmholtz Association (MDC), Berlin, Germany.
Priyavathi DhandapaniMax-Delbrück-Center for Molecular Medicine in the Helmholtz Association (MDC), Berlin, Germany.
Susann MatthesMax-Delbrück-Center for Molecular Medicine in the Helmholtz Association (MDC), Berlin, Germany.
Valentina MosienkoMax-Delbrück-Center for Molecular Medicine in the Helmholtz Association (MDC), Berlin, Germany.
Michael RotheLipidomix, Berlin, Germany.
Mihail TodirasMax-Delbrück-Center for Molecular Medicine in the Helmholtz Association (MDC), Berlin, Germany.
Julie SelfMax-Delbrück-Center for Molecular Medicine in the Helmholtz Association (MDC), Berlin, Germany.
Wolf-Hagen SchunckMax-Delbrück-Center for Molecular Medicine in the Helmholtz Association (MDC), Berlin, Germany.
Anja SchützMax-Delbrück-Center for Molecular Medicine in the Helmholtz Association (MDC), Berlin, Germany.
Michael BaderMax-Delbrück-Center for Molecular Medicine in the Helmholtz Association (MDC), Berlin, Germany.
Natalia AleninaMax-Delbrück-Center for Molecular Medicine in the Helmholtz Association (MDC), Berlin, Germany.ORCID 0000-0002-6071-5433
Max Delbrück Center · DELipidomix (Germany) · DESt Petersburg University · RU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Serotonin is an important signaling molecule in the periphery and in the brain. The hydroxylation of tryptophan is the first and rate-limiting step of its synthesis. In most vertebrates, two enzymes have been described to catalyze this step, tryptophan hydroxylase (TPH) 1 and 2, with expression localized to peripheral and neuronal cells, respectively. However, animals lacking both TPH isoforms still exhibit about 10% of normal serotonin levels in the blood demanding an additional source of the monoamine. In this study, we provide evidence by the gain and loss of function approaches in in vitro and in vivo systems, including stable-isotope tracing in mice, that phenylalanine hydroxylase (PAH) is a third TPH in mammals. PAH contributes to serotonin levels in the blood, and may be important as a local source of serotonin in organs in which no other TPHs are expressed, such as liver and kidney.

Indexed as

AnimalsBrainHepatocytesMiceSerotoninTryptophan HydroxylaseSerotoninTph1 protein, mouseTph2 protein, mouseTryptophan Hydroxylasephenylalanine hydroxylaseserotonintryptophan hydroxylase

Identifiers

PMID33993565
PMCPMC12315947
OpenAlexW3160677506

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.